ID   KEX1_TALMQ              Reviewed;         626 AA.
AC   B6QQZ9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   13-SEP-2023, entry version 58.
DE   RecName: Full=Pheromone-processing carboxypeptidase kex1;
DE            EC=3.4.16.6;
DE   AltName: Full=Carboxypeptidase D;
DE   Flags: Precursor;
GN   Name=kex1; ORFNames=PMAA_045500;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
CC   -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC       the C-terminal processing of the lysine and arginine residues from
CC       protein precursors. Promotes cell fusion and is involved in the
CC       programmed cell death (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal arginine or lysine
CC         residue.; EC=3.4.16.6;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; DS995904; EEA20727.1; -; Genomic_DNA.
DR   RefSeq; XP_002151727.1; XM_002151691.1.
DR   AlphaFoldDB; B6QQZ9; -.
DR   SMR; B6QQZ9; -.
DR   STRING; 441960.B6QQZ9; -.
DR   ESTHER; talmq-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   GlyCosmos; B6QQZ9; 4 sites, No reported glycans.
DR   VEuPathDB; FungiDB:PMAA_045500; -.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   PhylomeDB; B6QQZ9; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW   Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..626
FT                   /note="Pheromone-processing carboxypeptidase kex1"
FT                   /id="PRO_0000411934"
FT   TOPO_DOM        19..504
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        526..626
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          460..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        370
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        478
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   626 AA;  69623 MW;  C2B374719456DD9E CRC64;
     MLGKALLLLL SSPICAWAQS AADYYVKSIP GQPDGPLLKM HAGHVEVDAE TNGHLFFWHF
     QNRHIANRQR TILWLNGGPG CSSMDGALME IGPYRVKDDH TLIYNNGSWD EFANLLFVDQ
     PVGTGFSYVN TNSYLHDLDH VAAHMITFLE KWFAMFPEYE SDDLYIAGES YAGQYIPHIA
     RAIVERNKNI QRNQQHWPIK GLLIGNGWIS PRDQYPANLQ YAYAEGIVKE GTAIANELDG
     IEKSCDEQLN APGAGDLVDI RQCESILNKL LDLTRTSDDQ CINVYDIRLK DATCGNAWPP
     DLDQMTDYLR RADVGAALNL DNGKANGWTE CNNQVTANFR MGHNGVPSIQ LLPGLIESGV
     KVLLFSGDRD LICNHLGTES LIHNMKWSGG TGFETKPGVW APRRGWTFEG EAAGYYQQAR
     NLTYVLFYNA SHMVPYDFPR RTRDMVDRFI NVDIANIGGP PADSRLDGEK LPQTSVGNTT
     SSTSGTDQVD EAKLKDAEWK AYTKSGEAAL IVVIIGVSVW GFFIWRARQR AARDGTSPTK
     KGYRAVYQDG VDNNSSTDGA GLLSRFRNQS NSNSSRDLEA RDFDEAELDS LTPNLQNGHE
     RDHYVIGEED EDEDNDIGNG AKSSLH
//